P26883 (FKB1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A
Short name=PPIase FKBP1A
EC=5.2.1.8

Alternative name(s):
12 kDa FK506-binding protein
Short name=12 kDa FKBP
Short name=FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name=FKBP-1A
Immunophilin FKBP12
Rotamase

Gene names

Name:	Fkbp1a
Synonyms:	Fkbp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Inhibited by both FK506 and rapamycin.
Subunit structure	Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation By similarity. Interacts with ACVR1B and SMAD7. Interacts directly with RYR1, RYR2 and RYR3 By similarity. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Ref.6
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP1 subfamily. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell proliferation Inferred from mutant phenotype PubMed 14605212. Source: MGI cytokine-mediated signaling pathway Inferred from mutant phenotype PubMed 14605212. Source: MGI heart trabecula formation Inferred from mutant phenotype PubMed 9461216. Source: BHF-UCL muscle contraction Inferred from mutant phenotype PubMed 15289441. Source: MGI negative regulation of protein phosphatase type 2B activity Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of protein phosphorylation Inferred from direct assay PubMed 15467718. Source: MGI protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of ryanodine-sensitive calcium-release channel activity Inferred from mutant phenotype PubMed 9461216. Source: BHF-UCL release of sequestered calcium ion into cytosol Inferred from direct assay PubMed 12704193. Source: MGI response to caffeine Inferred from mutant phenotype PubMed 15289441. Source: MGI response to iron ion Inferred from electronic annotation. Source: Compara ventricular cardiac muscle tissue morphogenesis Inferred from mutant phenotype PubMed 9461216. Source: BHF-UCL
Cellular_component	axon Inferred from Biological aspect of Ancestor. Source: RefGenome axon terminus Inferred from electronic annotation. Source: Compara cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome sarcoplasmic reticulum membrane Inferred from direct assay PubMed 14592808. Source: MGI
Molecular_function	FK506 binding Inferred from direct assay Ref.1. Source: MGI peptidyl-prolyl cis-trans isomerase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 108	107	Peptidyl-prolyl cis-trans isomerase FKBP1A		PRO_0000075290
Regions
	Domain	20 – 108	89	PPIase FKBP-type
Amino acid modifications
	Modified residue	9	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26883 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 8C265ED5803F6987	FASTA	108	11,923
	10 20 30 40 50 60 MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT LGKQEVIRGW 70 80 90 100 EEGVAQMSVG QRAKLIISSD YAYGATGHPG IIPPHATLVF DVELLKLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA encoding murine FK506-binding protein (FKBP): nucleotide and deduced amino acid sequence." Nelson P.A., Lippke J.A., Murcko M.A., Rosborough S.L., Peattie D.A. Gene 109:255-258(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6 X CBA.
[2]	Shou W., Bao S., Mathews L.S., Matzuk M.M. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 129/Sv.
[3]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ILS and ISS.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Hippocampus.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[6]	"Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity." Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R. Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; RYR1 AND PROTEIN PHOSPHATASE 1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60203 mRNA. Translation: CAA42762.1. U65100, U65098, U65099 Genomic DNA. Translation: AAB17554.1. AF483488 mRNA. Translation: AAL90762.1. AF483489 mRNA. Translation: AAL90763.1. AK002777 mRNA. Translation: BAB22351.1. AK010693 mRNA. Translation: BAB27125.1. AK019362 mRNA. Translation: BAB31680.1. AK154751 mRNA. Translation: BAE32804.1. AK168333 mRNA. Translation: BAE40271.1. AK169186 mRNA. Translation: BAE40963.1. AK169242 mRNA. Translation: BAE41008.1. BC004671 mRNA. Translation: AAH04671.1.
IPI	IPI00266899.
PIR	JH0528.
RefSeq	NP_032045.1. NM_008019.2.
UniGene	Mm.278458. Mm.487732.
3D structure databases
ProteinModelPortal	P26883.
SMR	P26883. Positions 2-108.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29707N.
IntAct	P26883. 1 interaction.
PTM databases
PhosphoSite	P26883.
Proteomic databases
PaxDb	P26883.
PRIDE	P26883.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000044011; ENSMUSP00000037206; ENSMUSG00000032966.
GeneID	14225.
KEGG	mmu:14225.
Organism-specific databases
CTD	2280.
MGI	MGI:95541. Fkbp1a.
Phylogenomic databases
eggNOG	COG0545.
GeneTree	ENSGT00550000074272.
HOGENOM	HOG000154887.
HOVERGEN	HBG051623.
KO	K09568.
OMA	GNRSAGK.
OrthoDB	EOG42NJ1X.
Gene expression databases
ArrayExpress	P26883.
Bgee	P26883.
CleanEx	MM_FKBP1A.
Genevestigator	P26883.
GermOnline	ENSMUSG00000032966. Mus musculus.
Family and domain databases
InterPro	IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view]
PANTHER	PTHR10516. PTHR10516. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	285479.
SOURCE	Search...

Entry information

Entry name

FKB1A_MOUSE

Accession

Primary (citable) accession number: P26883
Secondary accession number(s): Q545E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program